High-throughput neuraminidase substrate specificity study of human and avian influenza A viruses.
High-throughput neuraminidase substrate specificity study of human and avian influenza A viruses.
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DOI:
10.1016/j.virol.2011.03.024
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发表时间:
2011-06-20
期刊:
影响因子:
3.7
通讯作者:
Chen X
中科院分区:
文献类型:
--
作者:
Li Y;Cao H;Dao N;Luo Z;Yu H;Chen Y;Xing Z;Baumgarth N;Cardona C;Chen X
Despite the importance of neuraminidase (NA) activity in effective infection by influenza A viruses, limited information exists about the differences of substrate preferences of viral neuraminidases from different hosts or from different strains. Using a high-throughput screening format and a library of twenty α2–3- or α2–6-linked para-nitrophenol-tagged sialylgalactosides, substrate specificity of NAs on thirty-seven strains of human and avian influenza A viruses was studied using intact viral particles. Neuraminidases of all viruses tested cleaved both α2–3- and α2–6-linked sialosides but preferred α2–3-linked ones and the activity was dependent on the terminal sialic acid structure. In contrast to NAs of other subtypes of influenza A viruses which did not cleave 2-keto-3-deoxy-D-glycero-D-galacto-nonulosonic acid (Kdn) or 5-deoxy Kdn (5d–Kdn), NAs of all N7 subtype viruses tested had noticeable hydrolytic activities on α2–3-linked sialosides containing Kdn or 5d–Kdn. Additionally, group 1 NAs showed efficient activity in cleaving N-azidoacetylneuraminic acid from α2 –3-linked sialoside.
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影响因子:
4
作者:
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通讯作者:
Varki, Ajit
影响因子:
3.7
作者:
PALESE, P;TOBITA, K;COMPANS, RW
通讯作者:
COMPANS, RW
影响因子:
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作者:
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影响因子:
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作者:
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DOI:
10.1073/pnas.160270697
发表时间:
2000-08-15
影响因子:
11.1
作者:
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通讯作者:
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